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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain V4))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; in homodimeric partnerUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Active sitei178 – 1781Proton acceptorUniRule annotation
Binding sitei180 – 1801SubstrateUniRule annotation
Metal bindingi204 – 2041Magnesium; via carbamate groupUniRule annotation
Metal bindingi206 – 2061MagnesiumUniRule annotation
Metal bindingi207 – 2071MagnesiumUniRule annotation
Active sitei296 – 2961Proton acceptorUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei329 – 3291SubstrateUniRule annotation
Sitei336 – 3361Transition state stabilizerUniRule annotation
Binding sitei381 – 3811SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMINF481448:GJEI-1289-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Synonyms:rbcLUniRule annotation
Ordered Locus Names:Minf_1264
OrganismiMethylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain V4))
Taxonomic identifieri481448 [NCBI]
Taxonomic lineageiBacteriaVerrucomicrobiaunclassified VerrucomicrobiaMethylacidiphilalesMethylacidiphilaceaeMethylacidiphilum
ProteomesiUP000009149: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_0000355750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysineUniRule annotation

Proteomic databases

PRIDEiB3DVG5.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi481448.Minf_1264.

Structurei

3D structure databases

ProteinModelPortaliB3DVG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B3DVG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIAGDGKAG AKKSRWSAGV TPYAEMGYYN ADYVPKDTDI LAAFRFVPQE
60 70 80 90 100
GVEPIEAGAA VAGESSTATW TVVWTDRLTA YEHYQGKCFR VEPVPGTNQY
110 120 130 140 150
IAFIAYDLDL FEEGSIANMS SSIIGNVFGF KALKSLRLED LRIPPHYVKT
160 170 180 190 200
FQGPAHGIMM EREYLNKYGR PLLGATVKPK LGLSAKNYGR VVYEALRGGL
210 220 230 240 250
DFTKDDENIN SQPFMRWRDR WLFCMEAVNK AMAETGEIKG HYLNVTAATM
260 270 280 290 300
EEMYERAEFA KELGSVIIMV DLTAGFTAIQ SMAKWCRKNG VLLHLHRAGH
310 320 330 340 350
STYTRQKIHG VNFRVIAKWM RLAGVDHIHA GTVVGKLEGD LHSVQGYYKT
360 370 380 390 400
LRTQYTEADP LLGLYFEQDW ASMPGVMPVA SGGIHAGQMH LLLSYLGEDT
410 420 430 440 450
ILQFGGGTIG HPDGIAAGAT ANRVAVEVMV QARNEGKDIL REGPEILEKA
460 470 480
CRWSPALAKA IETWKDISFE FESTDVPDAV AMPTIA
Length:486
Mass (Da):53,694
Last modified:July 22, 2008 - v1
Checksum:iA0A9CE650CA08146
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000975 Genomic DNA. Translation: ACD83318.1.
RefSeqiYP_001939916.1. NC_010794.1.

Genome annotation databases

EnsemblBacteriaiACD83318; ACD83318; Minf_1264.
GeneIDi6352199.
KEGGimin:Minf_1264.
PATRICi22491667. VBIMetInf111569_1320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000975 Genomic DNA. Translation: ACD83318.1.
RefSeqiYP_001939916.1. NC_010794.1.

3D structure databases

ProteinModelPortaliB3DVG5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi481448.Minf_1264.

Proteomic databases

PRIDEiB3DVG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD83318; ACD83318; Minf_1264.
GeneIDi6352199.
KEGGimin:Minf_1264.
PATRICi22491667. VBIMetInf111569_1320.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciMINF481448:GJEI-1289-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the extremely acidophilic methanotroph isolate V4, Methylacidiphilum infernorum, a representative of the bacterial phylum Verrucomicrobia."
    Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.
    , Feng L., Wang L., Alam M.
    Biol. Direct 3:26-26(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Isolate V4.

Entry informationi

Entry nameiRBL_METI4
AccessioniPrimary (citable) accession number: B3DVG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 22, 2008
Last modified: January 7, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.